Cbz-Leu-Ala-NH2 | 62074-75-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: Cbz-Leu-Ala-NH2
• 英文别名: Z-Leu-Ala-NH2；N-(N-benzyloxycarbonyl-L-leucyl)-L-alanine amide；N-(N-Benzyloxycarbonyl-L-leucyl)-L-alanin-amid；N-[(Benzyloxy)carbonyl]-L-leucyl-L-alaninamide；benzyl N-[(2S)-1-[[(2S)-1-amino-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate
• CAS: 62074-75-3
• 化学式: C₁₇H₂₅N₃O₄
• 分子量: 335.403
• InChiKey: SGQQEHYZSPWMOR-JSGCOSHPSA-N

物化性质

• 熔点：
  175-177 °C
• 沸点：
  598.8±45.0 °C(Predicted)
• 密度：
  1.152±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  24
• 可旋转键数：
  9
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  111
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Cbz-Leu-Ala-NH2 在 喹啉 、 sodium tetrahydroborate 、 三氟乙酸酐 作用下， 以 乙醚 为溶剂， 反应 2.17h， 生成 2-[(S)-2-((S)-2-Benzyloxycarbonylamino-4-methyl-pentanoylamino)-propionylamino]-3,3,3-trifluoro-propionic acid methyl ester
  参考文献：
  名称：

  通过三氟甲基取代的嘧啶并入α-三氟甲基α-氨基酸来修饰肽

  摘要：

  可以通过在三氟丙酮酸分别与N-保护的α-氨基酸酰胺和二肽酰胺反应时获得的嘧啶将α-三氟甲基取代的α-氨基酸引入肽的C-末端位置。

  DOI：

  10.1016/s0022-1139(00)80427-3
• 作为产物：
  描述：

  alkaline earth salt of/the/ methylsulfuric acid 在 氨 作用下， 生成 Cbz-Leu-Ala-NH2
  参考文献：
  名称：

  Polglase; Smith, Journal of the American Chemical Society, 1949, vol. 71, p. 3083

  摘要：

  DOI：

文献信息

• Enzymes in organic synthesis: use of subtilisin and a highly stable mutant derived from multiple site-specific mutations
  作者：Chi Huey Wong、S. T. Chen、William J. Hennen、Jeffrey A. Bibbs、Y. F. Wang、Jennifer L. C. Liu、Michael W. Pantoliano、Marc Whitlow、Philip N. Bryan

  DOI：10.1021/ja00159a006

  日期：1990.1

  wild-type enzyme to organic synthesis has been demonstrated in the regioselective acylation of nucleosides in anhydrous dimethylformamide (with 65-100% regioselectivity at the 5'-position), in the enantioselective hydrolysis of N-protected and unprotected common and uncommon amino acid esters inmore » water (with 85-98% enantioselectivity for the L-isomer), and in the synthesis of di- and oligopeptides

  发现通过六个位点特异性突变（Met50Phe、Gly169Ala、Asn76Asp、Gln206Cys、Tyr2l7Lys 和 Asn2l8Ser）衍生自枯草杆菌蛋白酶 BPN' 的枯草杆菌蛋白酶突变体（枯草杆菌蛋白酶 8350）在水溶液中比野生溶液中的稳定性高 100 倍在无水二甲基甲酰胺中比野生型稳定 50 倍。使用酯、硫酯和酰胺底物以及过渡态类似物抑制剂 Boc-Ala-Val-Phe-CFsub 3} 的动力学研究表明，野生型和突变型酶具有非常相似的特异性和催化作用特性。野生型酶的抑制常数 (Ki = 5.0 mu}M) 是突变酶 (Ki = 1.1 mu}M) 的约 5 倍，表明突变酶与反应过渡态的结合比野生型酶。该结果与观察到的相应酯和酰胺底物的速率常数一致；即，突变体的 ksub cat}/Ksub m} 值大于野生型酶的值。突变酶和野生型酶在有机合成中的应用已在无
• Chemo-Enzymatic Synthesis of Optically Active Amino Acids and Peptides
  作者：Shui-Tein Chen、Kung-Tsung Wang

  DOI：10.1002/jccs.199900046

  日期：1999.6

  AbstractThe industrial alkaline protease, alcalase, is stable and active in a high concentration of organic solvents and useful as a biocatalyst for (i) diastereoselective hydrolysis of peptide esters and preparation of racemization‐free peptides; (ii) selective incorporation of esters of D‐amino acid into peptides in t‐butanol via a selective hydrolysis of esters of D,L‐amino acid, followed by using the unhydrolyzed D‐esters as a nucleophile in a kinetically controlled peptide bond formation; (iii) resolution of esters of amino acid in 95% t‐butanol/5% water, followed by saponification of the unreacted esters to offer both enantiomers with high yield and optical purity; (iv) completely resolve amino‐acid esters with high yield and optical purity via in situ racemization of the unreacted antipode catalyzed by pyridoxal 5‐phosphate; (v) cryobioorganic synthesis of peptides with increased yields 15%–40% of peptide bond formation by reaction at 5 °C instead of 25–30 °C of a kinetically controlled enzymatic reaction in alcohols.
• α-Chymotrypsin-catalyzed peptide synthesis in frozen aqueous solution using N-protected amino acid carbamoylmethyl esters as acyl donors
  作者：Sayed Mohiuddin Abdus Salam、Ken-ichi Kagawa、Katsuhiro Kawashiro

  DOI：10.1016/j.tetasy.2005.10.042

  日期：2006.1

  A kinetically controlled peptide synthesis catalyzed by alpha-chymotrypsin was performed in frozen aqueous solution (ice, -24 degrees C). The yield of the peptide was significantly improved by the use of the carbamoylmethyl (Cam) ester as the acyl donor instead of the conventional ethyl ester. The peptide yield increased up to ca. 90% when N-benzyloxycarbonyl (CBZ)-Phe-OCam and H-Phe-NH2 were used as the acyl donor and nucleophile, respectively. Such an improvement of the peptide yield in ice was also observed in the coupling of other CBZ-amino acid Cam esters as acyl donors. Furthermore, this approach was applied to the synthesis of peptides containing D-amino acids. The peptides such as CBZ-D-Phe-Phe-NH2, CBZ-Phe-D-Phe-NH2 and CBZ-D-Phe-D-Phe-NH2 were also obtained in excellent to moderate yields in ice. A high diastereoselectivity towards the L-L peptide was observed when the racemic amino acid Cam ester was used as the acyl donor in ice. (c) 2005 Elsevier Ltd. All rights reserved.
• Kinetically controlled peptide bond formation in anhydrous alcohol catalyzed by the industrial protease alcalase
  作者：Shui Tein Chen、Shiah Yun Chen、Kung Tsung Wang

  DOI：10.1021/jo00051a052

  日期：1992.12

  The industrial alkaline protease alcalase has been found to be very stable (half life > 5 days in ethanol or 2-methyl-2-propanol) and active in alcoholic solvents (except methanol). Procedures have been developed for alcalase-catalyzed, kinetically controlled peptide bond formation in anhydrous alcohol(ethanol, 2-methyl-2-propanol). Studies of the selectivity of an alcalase-catalyzed reaction show that only L-amino acid acyl donors are substrates at the p-1 subsite of alcalase; at the p-1' subsite both D- and L-amino acid nucleophiles are substrates. Other amino compounds such as benzylamine and phenylhydrazine are good nucleophiles. Studies of the effect of the water content of the reaction solution on the yield in the synthesis of Moz-Phe-Leu-NH2 showed that the 95% yield obtained in anhydrous 2-methyl-2-propanol was decreased to 48% in 2-methyl-2-propanol containing 4.86% water.
• WONG, CHI-HUEY;CHEN, S. -T.;HENNEN, WILLIAM J.;BIBBS, JEFFREY A.;WANG, Y.+, J. AMER. CHEM. SOC., 112,(1990) N, C. 945-953
  作者：WONG, CHI-HUEY、CHEN, S. -T.、HENNEN, WILLIAM J.、BIBBS, JEFFREY A.、WANG, Y.+

  DOI：——

  日期：——